Rev7 is a versatile HORMA (Hop1, Rev7, Mad2) family adaptor protein with multiple roles in mitotic regulation and DNA damage response, and an essential accessory subunit of the translesion synthesis (TLS) DNA polymerase Pol? employed in replication of damaged DNA. Within Pol?, the two copies of Rev7 interact with the two Rev7-bonding motifs (RBM1 and RBM2) of the catalytic subunit Rev3 by a mechanism characteristic of HORMA proteins whereby the "safety-belt" loop of Rev7 closes on the top of the...
[NMR paper] Backbone and ILV side-chain NMR resonance assignments of the catalytic domain of human deubiquitinating enzyme USP7
Backbone and ILV side-chain NMR resonance assignments of the catalytic domain of human deubiquitinating enzyme USP7
Ubiquitin specific protease 7 (USP7) is a deubiquitinating enzyme, which removes ubiquitin tag from numerous protein substrates involved in diverse cellular processes such as cell cycle regulation, apoptosis and DNA damage response. USP7 affects stability, interaction network and cellular localization of its cellular and viral substrates by controlling their ubiquitination status. The large 41 kDa catalytic domain of USP7 harbors the active site of the enzyme. Here we present...
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[NMR paper] Unambiguous Side-Chain Assignments for Solid-State NMR Structure Elucidation of Nondeuterated Proteins via a Combined 5D/4D Side-Chain-to-Backbone Experiment
Unambiguous Side-Chain Assignments for Solid-State NMR Structure Elucidation of Nondeuterated Proteins via a Combined 5D/4D Side-Chain-to-Backbone Experiment
Owing to fast-magic-angle-spinning technology, proton-detected solid-state NMR has been facilitating the analysis of insoluble, crystalline, sedimented, and membrane proteins. However, potential applications have been largely restricted by limited access to side-chain resonances. The recent availability of spinning frequencies exceeding 100 kHz in principle now allows direct probing of all protons without the need for partial...
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[NMR paper] NMR 1H,13C, 15N backbone and 13C side chain resonance assignment of the G12C mutant of human K-Ras bound to GDP.
NMR 1H,13C, 15N backbone and 13C side chain resonance assignment of the G12C mutant of human K-Ras bound to GDP.
Related Articles NMR 1H,13C, 15N backbone and 13C side chain resonance assignment of the G12C mutant of human K-Ras bound to GDP.
Biomol NMR Assign. 2018 May 02;:
Authors: Sharma AK, Lee SJ, Rigby AC, Townson SA
Abstract
K-Ras is a key driver of oncogenesis, accounting for approximately 80% of Ras-driven human cancers. The small GTPase cycles between an inactive, GDP-bound and an active, GTP-bound state, regulated by...
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[NMR paper] NMR study of Met-1 human Angiogenin: (1)H, (13)C, (15)N backbone and side-chain resonance assignment.
NMR study of Met-1 human Angiogenin: (1)H, (13)C, (15)N backbone and side-chain resonance assignment.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--production.springer.de-OnlineResources-Logos-springerlink.gif Related Articles NMR study of Met-1 human Angiogenin: (1)H, (13)C, (15)N backbone and side-chain resonance assignment.
Biomol NMR Assign. 2016 Sep 13;
Authors: Tsika AC, Chatzileontiadou DS, Leonidas DD, Spyroulias GA
Abstract
Here, we report the high yield expression and preliminary structural...
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09-22-2016 06:31 AM
[NMR paper] (1)H, (13)C, (15)N backbone and side chain NMR resonance assignments of BPSL1050 from Burkholderia pseudomallei.
(1)H, (13)C, (15)N backbone and side chain NMR resonance assignments of BPSL1050 from Burkholderia pseudomallei.
Related Articles (1)H, (13)C, (15)N backbone and side chain NMR resonance assignments of BPSL1050 from Burkholderia pseudomallei.
Biomol NMR Assign. 2013 Apr 25;
Authors: Gaudesi D, Quilici G, Musco G
Abstract
BPSL1050 is a 13.9*kDa protein produced by the Gram-negative bacterium Burkholderia pseudomallei, the etiological agent of melioidosis. Immunodetection assays against sera patients using protein microarray suggest BPSL1050...
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Backbone and side chain NMR assignments for the intrinsically disordered cytoplasmic domain of human neuroligin-3.
Backbone and side chain NMR assignments for the intrinsically disordered cytoplasmic domain of human neuroligin-3.
Backbone and side chain NMR assignments for the intrinsically disordered cytoplasmic domain of human neuroligin-3.
Biomol NMR Assign. 2011 Jun 7;
Authors: Wood K, Paz A, Dijkstra K, Scheek RM, Otten R, Silman I, Sussman JL, Mulder FA
Neuroligins act as heterophilic adhesion molecules at neuronal synapses. Their cytoplasmic domains interact with synaptic scaffolding proteins, and have been shown to be intrinsically disordered. Here we...
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06-08-2011 11:30 AM
[NMR paper] Residual backbone and side-chain 13C and 15N resonance assignments of the intrinsic t
Residual backbone and side-chain 13C and 15N resonance assignments of the intrinsic transmembrane light-harvesting 2 protein complex by solid-state Magic Angle Spinning NMR spectroscopy.
Related Articles Residual backbone and side-chain 13C and 15N resonance assignments of the intrinsic transmembrane light-harvesting 2 protein complex by solid-state Magic Angle Spinning NMR spectroscopy.
J Biomol NMR. 2005 Apr;31(4):279-93
Authors: Gammeren AJ, Hulsbergen FB, Hollander JG, Groot HJ
This study reports the sequence specific chemical shifts...
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[NMR paper] Backbone and side-chain heteronuclear resonance assignments and hyperfine NMR shifts
Backbone and side-chain heteronuclear resonance assignments and hyperfine NMR shifts in horse cytochrome c.
Related Articles Backbone and side-chain heteronuclear resonance assignments and hyperfine NMR shifts in horse cytochrome c.
Protein Sci. 2003 Sep;12(9):2104-8
Authors: Liu W, Rumbley J, Englander SW, Wand AJ
The mutant of horse heart cytochrome c was expressed in E. coli during growth on isotopically enriched minimal media. Complete resonance assignments of both the diamagnetic reduced (spin zero) and paramagnetic oxidized (spin (1/2))...
Backbone and ILV side-chain methyl NMR resonance assignments of human Rev7/Rev3-RBM1 and Rev7/Rev3-RBM2 complexes
Linear Mode
